MRGBP promotes AR-mediated transactivation of KLK3 and TMPRSS2 via acetylation of histone H2A.Z in prostate cancer cells

S, Itó; Kayukawa, Naruhiro; Ueda, Takashi; Taniguchi, Hidefumi; Morioka, Yukako; Hongo, Fumiya; Ukimura, Osamu

doi:10.1016/j.bbagrm.2018.07.014

Cited by 23 publications

(28 citation statements)

References 25 publications

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“…For example, MRG15 is able to recognize H3K4me1 and H3K4me3 (Fig. 2c, [122]), Tip60 binds to H3K4me1 (Fig. 2c, [118]) and GAS41, via its YEAST domain, recognizes acetylated or succinylated histone tails (Fig.…”

Section: Mechanisms Of Loading and Removal Of The Histone Variant H2azmentioning

confidence: 99%

The histone variant H2A.Z in gene regulation

Giaimo

Ferrante

Herchenröther

et al. 2019

Epigenetics & Chromatin

242

179

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The histone variant H2A.Z is involved in several processes such as transcriptional control, DNA repair, regulation of centromeric heterochromatin and, not surprisingly, is implicated in diseases such as cancer. Here, we review the recent developments on H2A.Z focusing on its role in transcriptional activation and repression. H2A.Z, as a replication-independent histone, has been studied in several model organisms and inducible mammalian model systems. Its loading machinery and several modifying enzymes have been recently identified, and some of the long-standing discrepancies in transcriptional activation and/or repression are about to be resolved. The buffering functions of H2A.Z, as supported by genome-wide localization and analyzed in several dynamic systems, are an excellent example of transcriptional control. Posttranslational modifications such as acetylation and ubiquitination of H2A.Z, as well as its specific binding partners, are in our view central players in the control of gene expression. Understanding the key-mechanisms in either turnover or stabilization of H2A.Z-containing nucleosomes as well as defining the H2A.Z interactome will pave the way for therapeutic applications in the future.

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Section: Mechanisms Of Loading and Removal Of The Histone Variant H2azmentioning

confidence: 99%

The histone variant H2A.Z in gene regulation

Giaimo

Ferrante

Herchenröther

et al. 2019

Epigenetics & Chromatin

242

179

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“…We have shown that ongoing HDAC activity is responsible for removing H2A.Zac from the nuclear periphery at the onset of differentiation, and that HDAC activity is essential for differentiation to proceed. From analysis of the transcriptional activation and repression of the androgen receptor system (21,33), Giaimo (18) have proposed that H2A.Z, and especially ubiquitinated H2A.Z, can be repressive, but H2A.Z acetylation leads to its deubiquitination and consequent activation of genes. Our finding that the nuclear periphery is specifically and transiently enriched for H2A.Z acetylation in the early stages of pluripotency loss of human ES cells suggests that upon differentiation, many genes normally found at the periphery, a generally repressive compartment, may rapidly transit to an active state through the action of H2A.Z-specific acetyltransferases.…”

Section: Discussionmentioning

confidence: 99%

“…We reasoned that if histone modifications were enriched at the nuclear periphery, then the enzymes responsible for them may also be cytologically detectable in the same location. Previous work suggests that Tip60 is the primary HAT catalyzing H2A.Z acetylation (20,32,33), and while the identity of HDACs responsible for deacetylation of H2A.Zac is not known, it is likely to be a member of the "Class I" HDACs, HDAC1, HDAC2 or HDAC3 (34). HDAC1 and HDAC2 are known to be required for self-renewal and differentiation in ES and TS cells; however, the role of HDAC1 seems to be more critical (35)(36)(37).…”

Section: Characterization Of Fast Homogeneous Differentiation From Hmentioning

confidence: 99%

Sequential enrichment at the nuclear periphery of H2A.Zac and H3K9me2 accompanies pluripotency loss in human embryonic stem cells

Kafer

Rillo-Bohn

Carlton

2020

Preprint

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During the transition from pluripotency to a lineage-committed state, chromatin undergoes large-scale changes in structure to effect the required changes to the transcriptional program. This involves covalent modification of histone tails, replacement of histone variants, and alteration in the subnuclear position of genes, including associations with the nuclear periphery. Here, using high-resolution microscopy and quantitative image analysis, we surveyed a panel of histone variants and covalent modifications for changes in nuclear periphery association during differentiation of human embryonic stem cells to a trophoblast-like lineage. This differentiation process is rapid and homogeneous, facilitating the use of a relatively fine timecourse (12h, 24h, and 48h post-initiation) to enable detection of transient changes.With this scheme, we detected two modifications with significant changes in enrichment at the nuclear periphery: acetylation of histone variant H2A.Z, and dimethylation of histone H3 at lysine 9. We show that these chromatin marks increase specifically at the nuclear periphery in a sequential, complementary manner, with a H2A.Z acetylation preceding H3K9 dimethylation. The increase of H3K9 dimethylation occurred coincidentally with but independently of accumulation of Lamin A, since Lamin A -/-hES cells showed no changes in the localization pattern of H3K9 dimethylation. Inhibition of histone deacetylases led to persistent and increased H2A.Z acetylation at the periphery, and failure to differentiate. Our results show that a concerted dynamic change in the nature of peripheral chromatin is required for differentiation into the trophoblast state. Chromatin modification | H2A.Z | H3K9me2 | TrophoblastCorrespondence: carlton.petermark.3v@kyoto-u.ac.jp

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“…On the other hand, AT1G26470 encodes AtEAF7 in Arabidopsis, the homologous protein of yeast Eaf7 and human MRGBP (Table 1 and Figure 1) (Ito et al, 2018). AtEAF7 is also known as SNS1 (SnRK2-SUBSTRATE 1) since it is a target of SnRK2 (Umezawa et al, 2013), a protein kinase involved in abscisic acid (ABA) signaling pathway (Hirayama and Umezawa, 2010).…”

Section: Developmental and Stress-related Functions Associated To Hommentioning

confidence: 99%

Insights Into the Function of the NuA4 Complex in Plants

et al. 2020

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Chromatin remodeling plays a key role in the establishment and maintenance of gene expression patterns essential for plant development and responses to environmental factors. Post-translational modification of histones, including acetylation, is one of the most relevant chromatin remodeling mechanisms that operate in eukaryotic cells. Histone acetylation is an evolutionarily conserved chromatin signature commonly associated with transcriptional activation. Histone acetylation levels are tightly regulated through the antagonistic activity of histone acetyltransferases (HATs) and histone deacetylases (HDACs). In plants, different families of HATs are present, including the MYST family, which comprises homologs of the catalytic subunit of the Nucleosome Acetyltransferase of H4 (NuA4) complex in yeast. This complex mediates acetylation of histones H4, H2A, and H2A.Z, and is involved in transcriptional regulation, heterochromatin silencing, cell cycle progression, and DNA repair in yeast. In Arabidopsis and, other plant species, homologs for most of the yeast NuA4 subunits are present and although the existence of this complex has not been demonstrated yet, compelling evidence supports the notion that this type of HAT complex functions from mosses to angiosperms. Recent proteomic studies show that several Arabidopsis homologs of NuA4 components, including the assembly platform proteins and the catalytic subunit, are associated in vivo with additional members of this complex suggesting that a NuA4-like HAT complex is present in plants. Furthermore, the functional characterization of some Arabidopsis NuA4 subunits has uncovered the involvement of these proteins in the regulation of different plant biological processes. Interestingly, for most of the mutant plants deficient in subunits of this complex characterized so far, conspicuous defects in flowering time are observed, suggesting a role for NuA4 in the control of this plant developmental program. Moreover, the participation of Arabidopsis NuA4 homologs in other developmental processes, such as gametophyte development, as well as in cell proliferation and stress and hormone responses, has also been reported. In this review, we summarize the current state of knowledge on plant putative NuA4 subunits and discuss the latest progress concerning the function of this chromatin modifying complex.

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MRGBP promotes AR-mediated transactivation of KLK3 and TMPRSS2 via acetylation of histone H2A.Z in prostate cancer cells

Cited by 23 publications

References 25 publications

The histone variant H2A.Z in gene regulation

The histone variant H2A.Z in gene regulation

Sequential enrichment at the nuclear periphery of H2A.Zac and H3K9me2 accompanies pluripotency loss in human embryonic stem cells

Insights Into the Function of the NuA4 Complex in Plants

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